Francisco Tome
Research Associate Comparative MedicineDownloadHi-Res Photo
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Research Associate Comparative Medicine
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Yale Co-Authors
Frequent collaborators of Francisco Tome's published research.
Publications Timeline
A big-picture view of Francisco Tome's research output by year.
Joseph Schlessinger, PhD
Yoshihisa Suzuki
Sangwon Lee, PhD
Seong An, PhD
Irit Lax, PhD
Jungyuen Choi
16Publications
941Citations
Publications
2026
Cellular responses to FGF1 are modulated by palmitoylation of the docking protein FRS2α
An S, Suzuki Y, Mohanty J, Tome F, Lax I, Schlessinger J. Cellular responses to FGF1 are modulated by palmitoylation of the docking protein FRS2α. Proceedings Of The National Academy Of Sciences Of The United States Of America 2026, 123: e2605311123. PMID: 42054356, PMCID: PMC13143043, DOI: 10.1073/pnas.2605311123.Peer-Reviewed Original ResearchAltmetric
2023
Heparin is essential for optimal cell signaling by FGF21 and for regulation of βKlotho cellular stability
An S, Mohanty J, Tome F, Suzuki Y, Lax I, Schlessinger J. Heparin is essential for optimal cell signaling by FGF21 and for regulation of βKlotho cellular stability. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2219128120. PMID: 36745784, PMCID: PMC9962926, DOI: 10.1073/pnas.2219128120.Peer-Reviewed Original ResearchCitationsAltmetric
2020
FGF23 contains two distinct high-affinity binding sites enabling bivalent interactions with α-Klotho
Suzuki Y, Kuzina E, An SJ, Tome F, Mohanty J, Li W, Lee S, Liu Y, Lax I, Schlessinger J. FGF23 contains two distinct high-affinity binding sites enabling bivalent interactions with α-Klotho. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 31800-31807. PMID: 33257569, PMCID: PMC7749347, DOI: 10.1073/pnas.2018554117.Peer-Reviewed Original ResearchCitationsAltmetricMeSH KeywordsBinding SitesCalcinosisCell MembraneFibroblast Growth Factor-23Fibroblast Growth FactorsGlucuronidaseHEK293 CellsHumansHyperostosis, Cortical, CongenitalHyperphosphatemiaImmunoglobulin Fc FragmentsKlotho ProteinsMutationOsteomalaciaProtein BindingProtein DomainsProtein MultimerizationRecombinant Fusion ProteinsRickets, Hypophosphatemic
2019
Structures of ligand-occupied β-Klotho complexes reveal a molecular mechanism underlying endocrine FGF specificity and activity
Kuzina ES, Ung PM, Mohanty J, Tome F, Choi J, Pardon E, Steyaert J, Lax I, Schlessinger A, Schlessinger J, Lee S. Structures of ligand-occupied β-Klotho complexes reveal a molecular mechanism underlying endocrine FGF specificity and activity. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 7819-7824. PMID: 30944224, PMCID: PMC6475419, DOI: 10.1073/pnas.1822055116.Peer-Reviewed Original ResearchCitationsAltmetric
2018
Identification of a biologically active fragment of ALK and LTK-Ligand 2 (augmentor-α)
Reshetnyak AV, Mohanty J, Tomé F, Puleo DE, Plotnikov AN, Ahmed M, Kaur N, Poliakov A, Cinnaiyan AM, Lax I, Schlessinger J. Identification of a biologically active fragment of ALK and LTK-Ligand 2 (augmentor-α). Proceedings Of The National Academy Of Sciences Of The United States Of America 2018, 115: 8340-8345. PMID: 30061385, PMCID: PMC6099872, DOI: 10.1073/pnas.1807881115.Peer-Reviewed Original ResearchCitationsAltmetricStructures of β-klotho reveal a ‘zip code’-like mechanism for endocrine FGF signalling
Lee S, Choi J, Mohanty J, Sousa LP, Tome F, Pardon E, Steyaert J, Lemmon MA, Lax I, Schlessinger J. Structures of β-klotho reveal a ‘zip code’-like mechanism for endocrine FGF signalling. Nature 2018, 553: 501-505. PMID: 29342135, PMCID: PMC6594174, DOI: 10.1038/nature25010.Commentaries, Editorials and LettersCitationsAltmetricMeSH KeywordsBinding SitesCrystallography, X-RayExtracellular SpaceFibroblast Growth Factor-23Fibroblast Growth FactorsGlycoside HydrolasesHEK293 CellsHumansKlotho ProteinsLigandsMembrane ProteinsModels, MolecularProtein BindingProtein DomainsReceptors, Fibroblast Growth FactorSignal TransductionSubstrate Specificity
2016
Distinct cellular properties of oncogenic KIT receptor tyrosine kinase mutants enable alternative courses of cancer cell inhibition
Shi X, Sousa LP, Mandel-Bausch EM, Tome F, Reshetnyak AV, Hadari Y, Schlessinger J, Lax I. Distinct cellular properties of oncogenic KIT receptor tyrosine kinase mutants enable alternative courses of cancer cell inhibition. Proceedings Of The National Academy Of Sciences Of The United States Of America 2016, 113: e4784-e4793. PMID: 27482095, PMCID: PMC4995958, DOI: 10.1073/pnas.1610179113.Peer-Reviewed Original ResearchCitationsAltmetric
2015
Augmentor α and β (FAM150) are ligands of the receptor tyrosine kinases ALK and LTK: Hierarchy and specificity of ligand–receptor interactions
Reshetnyak AV, Murray PB, Shi X, Mo ES, Mohanty J, Tome F, Bai H, Gunel M, Lax I, Schlessinger J. Augmentor α and β (FAM150) are ligands of the receptor tyrosine kinases ALK and LTK: Hierarchy and specificity of ligand–receptor interactions. Proceedings Of The National Academy Of Sciences Of The United States Of America 2015, 112: 15862-15867. PMID: 26630010, PMCID: PMC4702955, DOI: 10.1073/pnas.1520099112.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords
2014
The Strength and Cooperativity of KIT Ectodomain Contacts Determine Normal Ligand-Dependent Stimulation or Oncogenic Activation in Cancer
Reshetnyak AV, Opatowsky Y, Boggon TJ, Folta-Stogniew E, Tome F, Lax I, Schlessinger J. The Strength and Cooperativity of KIT Ectodomain Contacts Determine Normal Ligand-Dependent Stimulation or Oncogenic Activation in Cancer. Molecular Cell 2014, 57: 191-201. PMID: 25544564, PMCID: PMC4764128, DOI: 10.1016/j.molcel.2014.11.021.Peer-Reviewed Original ResearchCitationsAltmetricMeSH KeywordsAnimalsBaculoviridaeBinding SitesCrystallography, X-RayEnzyme ActivationHumansLigandsMiceModels, MolecularMutationNeoplasmsNIH 3T3 CellsProtein BindingProtein FoldingProtein Interaction Domains and MotifsProtein MultimerizationProtein Structure, SecondaryProto-Oncogene Proteins c-kitRecombinant ProteinsSf9 CellsSpodopteraStructure, domain organization, and different conformational states of stem cell factor-induced intact KIT dimers
Opatowsky Y, Lax I, Tomé F, Bleichert F, Unger VM, Schlessinger J. Structure, domain organization, and different conformational states of stem cell factor-induced intact KIT dimers. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 1772-1777. PMID: 24449920, PMCID: PMC3918759, DOI: 10.1073/pnas.1323254111.Peer-Reviewed Original ResearchCitationsAltmetric
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